Hesperidinase (Rhamnosidase B) from Thermomicrobia sp.

rham143

280,00

A Thermostable α-L-rhamnosidase from Thermomicrobia sp.


SKU: rham143.
Category: .

Hard to decide? Ask your friends

Description

rham143A Thermostable α-L-rhamnosidase that catalyzes the cleavage of the bond between terminal L(+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is also very active on naringin. L-Rhamnose or its derivatives is a suitable chiral structural component and can be used for the synthesis of pharmaceutical products, plant protection agents and the preparation of fragrances in the foodstuffs and perfume industries.

 

Available as 100 units. Shipping within a week, shipping and handling charges additional to price listed below.

For purchase select product and add to cart above. We accept payments with credit cards via PayPal or direct bank transfer. Shipping within a week, shipping and handling charges additional to price listed.

Product : Rham143 | Hesperedinase 100 Units | Price : 280.00 EUR

For further information read more below or download the product sheet (pdf format).

Mode of action: The enzyme catalyzes the cleavage of the bond between terminal L(+)-rhamnose and the aglycone of rhamnose-containing glycosides. Hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides, Naringin, Hesperdin and Rutin.

Unit Definition: One unit (U) of enzyme activity is the amount that leads to the release of 1 µmol of p-nitro-phenyl-α-L-rhamnopyranoside (pnpR)  per minute.

Rham143 enzyme activity vs. temperatureTemperature Optimum: The enzyme in relatively active in a rather broad temperature range (45-75°C)with optimum around 65°C (Figure 1)

 Rham143 enzyme activity vs. pH

pH Optimum: pH range is about 4.5-9 with optimum about pH 7.5

 

 

Substrate specificity: Hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides, Naringin, Hesperdin and Rutin.

Rham143 Substrate specificity

Unit Assay Conditions:  Rhaminosidase activity was routinely determined in a 100mM KPO4 pH 7.5 buffer for 10 minutes with 2.0mM  final conc. of pnpR.

References:

1) Birgisson, H., Hreggvidsson, G. O., Fridjónsson, O. H., Mort, A., Kristjánsson, J. K., Mattiasson, B.,  Two new thermostable α-L-rhmnosidases from a novel thermophilic bacterium.  Enzyme and Microbial Technology 2004;34:561-571.

2) Birgisson, H.,  Wheat, J. O., Hreggvidsson, G. O., Kristjánsson, J. K., Mattiasson, B.  Immobilization of a recombinant Escherichia coli producing a thermostable α-l-rhamnosidase: Creation of a bioreactor for hydrolyses of naringin.   Enzyme and Microbial Technology 2007;40:1181-1187

Additional information

Unit size and price

100 units – EUR 280